7RR3

Structure of Deep-Sea Phage NrS-1 Primase-Polymerase N300 in complex with calcium and ddCTP

7RR3 の概要

• エントリーDOI: 10.2210/pdb7rr3/pdb
• 関連するPDBエントリー: 7RR4
• 分子名称: Primase, CALCIUM ION, 2',3'-DIDEOXYCYTIDINE 5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: primpol, denovo, polymerase, replication
• 由来する生物種: Nitratiruptor phage NrS-1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33740.80

構造登録者

Wang, L.,Yu, C.,Sliz, P. (登録日: 2021-08-09, 公開日: 2022-01-12, 最終更新日: 2024-11-13)

主引用文献

Huang, F.,Lu, X.,Yu, C.,Sliz, P.,Wang, L.,Zhu, B.
Molecular Dissection of the Primase and Polymerase Activities of Deep-Sea Phage NrS-1 Primase-Polymerase.
Front Microbiol, 12:766612-766612, 2021

PubMed Abstract: PrimPols are a class of primases that belong to the archaeo-eukaryotic primase (AEP) superfamily but have both primase and DNA polymerase activities. Replicative polymerase from NrS-1 phage (NrSPol) is a representative of the PrimPols. In this study, we identified key residues for the catalytic activity of NrSPol and found that a loop in NrSPol functionally replaces the zinc finger motif that is commonly found in other AEP family proteins. A helix bundle domain (HBD), conserved in the AEP superfamily, was recently reported to bind to the primase recognition site and to be crucial for initiation of primer synthesis. We found that NrSPol can recognize different primase recognition sites, and that the initiation site for primer synthesis is not stringent, suggesting that the HBD conformation is flexible. More importantly, we found that although the HBD-inactivating mutation impairs the primase activity of NrSPol, it significantly enhances the DNA polymerase activity, indicating that the HBD hinders the DNA polymerase activity. The conflict between the primase activity and the DNA polymerase activity in a single protein with the same catalytic domain may be one reason for why DNA polymerases are generally unable to synthesize DNA .

PubMed: 34975792
DOI: 10.3389/fmicb.2021.766612

実験手法

X-RAY DIFFRACTION (2.24 Å)